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Q12874 (SF3A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Splicing factor 3A subunit 3
Alternative name(s):
SF3a60
Spliceosome-associated protein 61
Short name=SAP 61
Gene names
Name:SF3A3
Synonyms:SAP61
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex.

Subunit structure

Identified in the spliceosome C complex. Component of splicing factor SF3A which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62, SF3A1/SAP114. SF3A associates with the splicing factor SF3B and a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex (U2 snRNP). Interacts with SF3A1, through its N-terminal region. Ref.8 Ref.19

Subcellular location

Nucleus speckle.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the SF3A3 family.

Contains 1 matrin-type zinc finger.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ORFQ9Q2G43EBI-1051880,EBI-6248094From a different organism.
SF3A1Q154592EBI-1051880,EBI-1054743

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Splicing factor 3A subunit 3
PRO_0000174318

Regions

Zinc finger406 – 43732Matrin-type
Compositional bias354 – 3629Poly-Glu

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6 Ref.11 Ref.18
Modified residue2991Phosphoserine Ref.13
Modified residue3651Phosphoserine Ref.10 Ref.13 Ref.16
Modified residue3671Phosphoserine Ref.10 Ref.13 Ref.16
Modified residue3691Phosphoserine Ref.10 Ref.13 Ref.16
Glycosylation1191N-linked (GlcNAc...) Ref.12

Experimental info

Sequence conflict1761E → G in CAA57388. Ref.2

Secondary structure

... 501
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12874 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 6E6F6EA17777E1E2

FASTA50158,849
        10         20         30         40         50         60 
METILEQQRR YHEEKERLMD VMAKEMLTKK STLRDQINSD HRTRAMQDRY MEVSGNLRDL 

        70         80         90        100        110        120 
YDDKDGLRKE ELNAISGPNE FAEFYNRLKQ IKEFHRKHPN EICVPMSVEF EELLKARENP 

       130        140        150        160        170        180 
SEEAQNLVEF TDEEGYGRYL DLHDCYLKYI NLKASEKLDY ITYLSIFDQL FDIPKERKNA 

       190        200        210        220        230        240 
EYKRYLEMLL EYLQDYTDRV KPLQDQNELF GKIQAEFEKK WENGTFPGWP KETSSALTHA 

       250        260        270        280        290        300 
GAHLDLSAFS SWEELASLGL DRLKSALLAL GLKCGGTLEE RAQRLFSTKG KSLESLDTSL 

       310        320        330        340        350        360 
FAKNPKSKGT KRDTERNKDI AFLEAQIYEY VEILGEQRHL THENVQRKQA RTGEEREEEE 

       370        380        390        400        410        420 
EEQISESESE DEENEIIYNP KNLPLGWDGK PIPYWLYKLH GLNINYNCEI CGNYTYRGPK 

       430        440        450        460        470        480 
AFQRHFAEWR HAHGMRCLGI PNTAHFANVT QIEDAVSLWA KLKLQKASER WQPDTEEEYE 

       490        500 
DSSGNVVNKK TYEDLKRQGL L 

« Hide

References

« Hide 'large scale' references
[1]"Specific protein-protein interactions between the essential mammalian spliceosome-associated proteins SAP 61 and SAP 114."
Chiara M.D., Champion-Arnaud P., Buvoli M., Nadal-Ginard B., Reed R.
Proc. Natl. Acad. Sci. U.S.A. 91:6403-6407(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cervix adenocarcinoma.
[2]"Splicing factor SF3a60 is the mammalian homologue of PRP9 of S.cerevisiae: the conserved zinc finger-like motif is functionally exchangeable in vivo."
Kraemer A., Legrain P., Mulhauser F., Groening K., Brosi R., Bilbe G.
Nucleic Acids Res. 22:5223-5228(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cervix adenocarcinoma.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye and Lung.
[6]Bienvenut W.V.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-9; 265-273 AND 292-303, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[7]"Functional association of U2 snRNP with the ATP-independent spliceosomal complex E."
Das R., Zhou Z., Reed R.
Mol. Cell 5:779-787(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE SPLICEOSOME.
[8]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[9]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119.
Tissue: Liver.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-365; SER-367 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP."
Kuwasako K., He F., Inoue M., Tanaka A., Sugano S., Guntert P., Muto Y., Yokoyama S.
Structure 14:1677-1689(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 71-107 IN COMPLEX WITH SF3A1, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08815 mRNA. Translation: AAA19625.1.
X81789 mRNA. Translation: CAA57388.1.
AL603790 Genomic DNA. Translation: CAH69930.1.
CH471059 Genomic DNA. Translation: EAX07304.1.
CH471059 Genomic DNA. Translation: EAX07305.1.
BC002395 mRNA. Translation: AAH02395.1.
BC011523 mRNA. Translation: AAH11523.1.
PIRA55749.
RefSeqNP_006793.1. NM_006802.2.
UniGeneHs.77897.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DT7NMR-A71-107[»]
ProteinModelPortalQ12874.
SMRQ12874. Positions 71-107.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116146. 57 interactions.
DIPDIP-882N.
IntActQ12874. 13 interactions.
MINTMINT-1467744.
STRING9606.ENSP00000362110.

PTM databases

PhosphoSiteQ12874.

Polymorphism databases

DMDM17380310.

Proteomic databases

PaxDbQ12874.
PeptideAtlasQ12874.
PRIDEQ12874.

Protocols and materials databases

DNASU10946.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373019; ENSP00000362110; ENSG00000183431.
GeneID10946.
KEGGhsa:10946.
UCSCuc001cci.3. human.

Organism-specific databases

CTD10946.
GeneCardsGC01M038422.
HGNCHGNC:10767. SF3A3.
HPAHPA032054.
MIM605596. gene.
neXtProtNX_Q12874.
PharmGKBPA35685.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5188.
HOGENOMHOG000160935.
HOVERGENHBG054452.
InParanoidQ12874.
KOK12827.
OMAYLDLHEC.
OrthoDBEOG77HDDF.
PhylomeDBQ12874.
TreeFamTF315227.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ12874.
BgeeQ12874.
CleanExHS_SF3A3.
GenevestigatorQ12874.

Family and domain databases

InterProIPR024598. DUF3449.
IPR021966. SF3a60_bindingd.
IPR015880. Znf_C2H2-like.
IPR000690. Znf_C2H2_matrin.
[Graphical view]
PfamPF11931. DUF3449. 1 hit.
PF12108. SF3a60_bindingd. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS50171. ZF_MATRIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSF3A3. human.
EvolutionaryTraceQ12874.
GeneWikiSF3A3.
GenomeRNAi10946.
NextBio41589.
PROQ12874.
SOURCESearch...

Entry information

Entry nameSF3A3_HUMAN
AccessionPrimary (citable) accession number: Q12874
Secondary accession number(s): D3DPT5, Q15460, Q5VT87
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM